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Cited by 22Proteins in Food SystemsProtein Hydrolysis and Bioactive PeptidesProtein purification and stability

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Salt Solubilization Coupled with Membrane Filtration-Impact on the Structure/Function of Chickpea Compared to Pea Protein

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Yaputri, Brigitta P., Bu, Fan, Ismail, Baraem P.·2023·Foods
DOI 10.3390/foods12081694PMC PMC10137475
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Abstract

The demand for pulse proteins as alternatives to soy protein has been steeply increasing over the past decade. However, the relatively inferior functionality compared to soy protein is hindering the expanded use of pulse proteins, namely pea and chickpea protein, in various applications. Harsh extraction and processing conditions adversely impact the functional performance of pea and chickpea protein. Therefore, a mild protein extraction method involving salt extraction coupled with ultrafiltration (SE-UF) was evaluated for the production of chickpea protein isolate (ChPI). The produced ChPI was compared to pea protein isolate (PPI) produced following the same extraction method in terms of functionality and feasibility of scaling. Scaled-up (SU) ChPI and PPI were produced under industrially relevant settings and evaluated in comparison to commercial pea, soy, and chickpea protein ingredients. Controlled scaled-up production of the isolates resulted in mild changes in protein structural characteristics and comparable or improved functional properties. Partial denaturation, modest polymerization, and increased surface hydrophobicity were observed in SU ChPI and PPI compared to the benchtop counterparts. The unique structural characteristics of SU ChPI, including its ratio of surface hydrophobicity and charge, contributed to superior solubility at both a neutral and acidic pH compared to both commercial soy protein and pea protein isolates (cSPI and cPPI) and significantly outperformed cPPI in terms of gel strength. These findings demonstrated both the promising scalability of SE-UF and the potential of ChPI as a functional plant protein ingredient.

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Figure 1 SDS-PAGE gel protein profile visualization of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, and SU ChPI), as well as commercial PPI, PPC, and ChPC under non-reducing (a) and reducing (b) conditions. Lane 1: Molecular weight (MW) marker; Lane 2, 3: cPPI and cPPC; Lane 4, 5: PPI and SU PPI, Lane 6: cChPC; Lane 7, 8: ChPI and SU ChPI. Lox: lipoxygenase; Cs: convicilin subunits; Lm: legumin monomer; Vs: vicilin subunits; Lsα: legumin acidic subunits, Lsβ: legumin basic subunits; Vsf: vicilin subunit fractions due to post-translational cleavages.
Figure 1 SDS-PAGE gel protein profile visualization of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, and SU ChPI), as well as commercial PPI, PPC, and ChPC under non-reducing (a) and reducing (b) conditions. Lane 1: Molecular weight (MW) marker; Lane 2, 3: cPPI and cPPC; Lane 4, 5: PPI and SU PPI, Lane 6: cChPC; Lane 7, 8: ChPI and SU ChPI. Lox: lipoxygenase; Cs: convicilin subunits; Lm: legumin monomer; Vs: vicilin subunits; Lsα: legumin acidic subunits, Lsβ: legumin basic subunits; Vsf: vicilin subunit fractions due to post-translational cleavages.CC BY · PubMed Central
Figure 2 SDS-PAGE gel protein profile visualization of high solid (HS) and low solid (LS) fractions of SU PPI compared to that of cPPI and SU ChPI compared to that of cChPC under non-reducing (lane 2–5) and reducing (lane 6–9) conditions. Lane 1: Molecular weight (MW) marker; Lane 2, 6: SU PPI HS; Lane 3, 7: SU PPI LS; Lane 4, 8: SU ChPI HS; Lane 5, 9: SU ChPI LS. Lox: lipoxygenase; Cs: convicilin subunits; Lm: legumin monomer; Vs: vicilin subunits; Lsα: legumin acidic subunits, Lsβ: legumin basic subunits; Vsf: vicilin subunit fractions due to post-translational cleavages.
Figure 2 SDS-PAGE gel protein profile visualization of high solid (HS) and low solid (LS) fractions of SU PPI compared to that of cPPI and SU ChPI compared to that of cChPC under non-reducing (lane 2–5) and reducing (lane 6–9) conditions. Lane 1: Molecular weight (MW) marker; Lane 2, 6: SU PPI HS; Lane 3, 7: SU PPI LS; Lane 4, 8: SU ChPI HS; Lane 5, 9: SU ChPI LS. Lox: lipoxygenase; Cs: convicilin subunits; Lm: legumin monomer; Vs: vicilin subunits; Lsα: legumin acidic subunits, Lsβ: legumin basic subunits; Vsf: vicilin subunit fractions due to post-translational cleavages.CC BY · PubMed Central
Figure 3 Protein gel strength of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, SU ChPI), as well as commercial SPI, PPI, PPC, and cChPC. An asterisk (*) denotes sample not analyzed due to high viscosity during sample solubilization. Error bars represent standard error (n = 3). Lowercase and uppercase letters above the bars denote significant differences among the samples evaluated at 15% and 20% protein concentration, respectively, according to the Tukey-Kramer multiple means comparison test (p < 0.05).
Figure 3 Protein gel strength of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, SU ChPI), as well as commercial SPI, PPI, PPC, and cChPC. An asterisk (*) denotes sample not analyzed due to high viscosity during sample solubilization. Error bars represent standard error (n = 3). Lowercase and uppercase letters above the bars denote significant differences among the samples evaluated at 15% and 20% protein concentration, respectively, according to the Tukey-Kramer multiple means comparison test (p < 0.05).CC BY · PubMed Central
Figure 4 Protein emulsion capacity, EC, (a) emulsion activity index, EAI, (b) and emulsion stability, ES, (c) of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, SU ChPI), as well as commercial SPI, PPI, PPC, and cChPC. Error bars represent standard error (n = 3). Lowercase letters above the bars denote significant differences among the samples, according to the Tukey-Kramer multiple means comparison test (p < 0.05).
Figure 4 Protein emulsion capacity, EC, (a) emulsion activity index, EAI, (b) and emulsion stability, ES, (c) of benchtop and scaled-up pea and chickpea protein isolates (PPI, SU PPI, ChPI, SU ChPI), as well as commercial SPI, PPI, PPC, and cChPC. Error bars represent standard error (n = 3). Lowercase letters above the bars denote significant differences among the samples, according to the Tukey-Kramer multiple means comparison test (p < 0.05).CC BY · PubMed Central

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Citations

Cites

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Metadata

Authors
Yaputri, B. P., Bu, F., & Ismail, B. P.
Affiliations
University of Minnesota (US)
Corresponding author
Ismail, Baraem P.
ORCID
Venue
Foods
Publisher
MDPI AG
Published
2023-04-19
Volume
12
Issue
8
Pages
1694
ISSN
2304-8158 (ISSN-L)
DOI
10.3390/foods12081694
PMC
PMC10137475
OpenAlex
W4366414682
Cited by
22
References
6
Citations by year
2026: 11 · 2025: 4 · 2024: 6 · 2023: 1
FWCI
2.92
Type
journal article
Language
en
Open access
Licence
Locations
  • Foods (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
Food Institute (GFI) nonprofit organization
Topics
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Protein Hydrolysis and Bioactive Peptides
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
Keywords
chickpea protein isolate, pea protein isolate, salt extraction, ultrafiltration, legume protein, protein functional properties, protein structure, surface hydrophobicity, protein solubility, gel strength

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Yaputri, B. P., Bu, F., & Ismail, B. P. (2023). Salt Solubilization Coupled with Membrane Filtration-Impact on the Structure/Function of Chickpea Compared to Pea Protein. Foods. https://doi.org/10.3390/foods12081694